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Yasu S. Morita

Assistant Professor

Research areas include infectious diseases, bacterial pathogenesis, tuberculosis, nontuberculous mycobacteria diseases, biogenesis of cell membrane and cell wall, microbial metabolism of lipids and glycans, chemotherapy, small molecule screening, and target discovery for antibiotics.

Current Research

My research group focuses on combating infectious diseases such as tuberculosis (TB) and leprosy by searching for new drug targets and designing assays to identify new antibiotics. Development of new anti-TB drugs will save millions of lives that succumb to death every year. Multi-drug resistant strains of TB pathogens are becoming more and more widespread, and co-infection with HIV, which is extremely difficult to treat, is becoming common; thus the urgent need for new antibiotics. We focus our research on sugar metabolism because sugars play key roles in creating surface coat of TB pathogens, making them naturally resistant to common antibiotics. While various types of sugars are needed to create the surface coat, there are not enough sugars in the environment where these bacteria thrive. TB pathogens must make these sugar molecules by themselves, thus metabolic pathways that produce these sugars are excellent targets for antibiotic screening.

Another strategy to identify potential drug targets is to investigate sugar metabolism in the context of biofilm formation. Biofilms have been implicated in the spread of diseases caused by bacteria related to TB pathogens. These diseases are collectively called nontuberculous mycobacteria (NTM) diseases, which is more common than TB in developed countries such as the US. NTM diseases are difficult to control due to the lack of effective antibiotics and the ability of the bacteria to form biofilms. We recently found that one of lipid-linked sugars that decorate the surface membrane of bacterial cells is critical for biofilm formation. We are currently investigating how this unique surface sugar coat is important for biofilm formation at the molecular level.

Learn more at www.micro.umass.edu/faculty-and-research/yasu-morita

Academic Background

  • PhD, Johns Hopkins University
  • Post-doctoral training, University of Melbourne/Osaka University
Eagen WJ, Baumoel LR, Osman SH, Rahlwes K, Morita YS* (2018) Deletion of PimE mannosyltransferase results in increased copper sensitivity in Mycobacterium smegmatis. FEMS Microbiol Lett. 365(6), fny025.
Hayashi JM, Richardson K, Melzer ES, Sandler SJ, Aldridge BB, Siegrist MS, Morita YS* (2018) Stress-induced reorganization of mycobacterial membrane domain. mBio. 9(1), e01823-17.
Rahlwes KC, Ha SA, Motooka D, Mayfield JA, Baumoel LR, Strickland JN, Torres-Ocampo AP, Nakamura S, Morita YS* (2017) The cell envelope-associated phospholipid-binding protein LmeA is required for mannan polymerization in mycobacteria. J Biol Chem. 292(42),17407-17417.
Hayashi, J.M., Luo, C.-Y., Mayfield, J.A., Hsu, T., Fukuda, T., Walfield, A.L., Giffen, S.R., Leszyk, J., Baer, C.E., Bennion, O.T., Madduri, A., Shaffer, S.A., Aldridge, B.B., Sassetti, C.M., Sandler, S.J., Kinoshita, T., Moody, D.B. and Morita, Y.S.* (2016) Spatially distinct and metabolically active membrane domain in mycobacteria. Proc. Natl. Acad. Sci. USA, 113, 5400-5.
Nakayama, H., Kurihara, H., Morita, Y.S., Kinoshita, T., Mauri, L., Prinetti, A., Sonnino, S., Yokoyama, N., Ogawa, H., Takamori, K., and Iwabuchi, K. (2016) Lipoarabinomannan binding to lactosylceramide in lipid rafts is essential for the phagocytosis of mycobacteria by human neutrophils. Sci. Signal., 9, ra101.
Fukuda, T., Matsumura, T., Ato, M., Hamasaki, M., Nishiuchi, Y., Murakami, Y., Maeda, Y., Yoshimori, T., Matsumoto, S., Kobayashi, K., Kinoshita, T., and Morita, Y.S. (2013) Critical roles for lipomannan and lipoarabinomannan in cell wall integrity of mycobacteria and pathogenesis of tuberculosis. mBio, 4, e00472-12.
Morita, Y.S., Fukuda, T., Sena, C.B., Yamaryo-Botte, Y., McConville, M.J., and Kinoshita, T. (2011) Inositol lipid metabolism in mycobacteria: biosynthesis and regulatory mechanisms. Biochim. Biophys. Acta, 1810, 630-41.
Sena, C.B., Fukuda, T., Miyanagi, K., Matsumoto, S., Kobayashi, K., Murakami, Y., Maeda, Y., Kinoshita, T., and Morita, Y.S. (2010) Controlled expression of branch-forming mannosyltransferase is critical for mycobacterial lipoarabinomannan biosynthesis. J. Biol. Chem., 285, 13326-36.
Ishikawa, E., Ishikawa, T., Morita, Y.S., Toyonaga, K., Yamada, H., Takeuchi, O., Kinoshita, T., Akira, S., Yoshikai, Y., and Yamasaki, S. (2009) Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle: Mincle is a receptor for mycobacterial glycolipid. J. Exp. Med., 206, 2879-88.
Morita, Y.S., Sena, C.B., Waller, R.F., Kurokawa, K., Sernee, M.F., Nakatani, F., Haites, R.E., Billman-Jacobe, H., McConville, M.J., Maeda, Y., and Kinoshita, T. (2006) PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of phosphatidylinositol mannoside in mycobacteria. J. Biol. Chem., 281, 25143-25155.
Contact Info

Department of Microbiology
LSL1 N233
240 Thatcher Road
Amherst, MA 01003-9292

(413) 545-4604